Reviewed, UniProtKB/Swiss-Prot Q99497 (PARK7_HUMAN)

Names and origin

Protein names

Recommended name:
    Protein DJ-1
Alternative name(s):
    Oncogene DJ1
    Parkinson disease protein 7

Gene names

Name:

PARK7

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	189 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Acts as a positive regulator of androgen receptor-dependent transcription. May function as a redox-sensitive chaperone and as a sensor for oxidative stress. Prevents aggregation of SNCA. Protects neurons against oxidative stress and cell death. Plays a role in fertilization. Has no proteolytic activity. Has cell-growth promoting activity and transforming activity. Ref.1 Ref.9 Ref.12 Ref.16 Ref.18 Ref.23 Ref.25
Subunit structure	Homodimer. Binds EFCAB6/DJBP and PIAS2. Part of a ternary complex containing PARK7, EFCAB6/DJBP and AR. Ref.23 Ref.10 Ref.20 Ref.21 Ref.22 Ref.24
Subcellular location	Nucleus. Cytoplasm. Note: Associated with mitochondria in some cells, particularly after oxidative stress. Detected in tau inclusions in brains from neurodegenerative disease patients. Ref.1 Ref.9 Ref.18 Ref.25 Ref.10 Ref.13 Ref.14 Ref.27
Tissue specificity	Highly expressed in pancreas, kidney, skeletal muscle, liver, testis and heart. Detected at slightly lower levels in placenta and brain. Detected in astrocytes, Sertoli cells, spermatogonia, spermatids and spermatozoa. Ref.1 Ref.13 Ref.14 Ref.15
Induction	By ultraviolet irradiation. Ref.18
Post-translational modification	Sumoylated on Lys-130 by PIAS2 or PIAS4; which is enhanced after ultraviolet irradiation and essential for cell-growth promoting activity and transforming activity. Ref.18
Involvement in disease	Defects in PARK7 are the cause of autosomal recessive early-onset Parkinson disease 7 (PARK7) [MIM:606324, 168600]. Parkinson disease (PD) is a complex, multifactorial disorder that typically manifests after the age of 50 years, although early-onset cases (before 50 years) are known. PD generally arises as a sporadic condition but is occasionally inherited as a simple mendelian trait. Although sporadic and familial PD are very similar, inherited forms of the disease usually begin at earlier ages and are associated with atypical clinical features. PD is characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. PARK7 is characterized by onset before 40 years, slow progression and initial good response to levodopa. Ref.10 Ref.27 Ref.11 Ref.26 Ref.29 Ref.30 Ref.31 Defects in PARK7 influences susceptibility to amyotrophic lateral sclerosis-parkinsonism/dementia complex type 2 [MIM:105500]; also called amyotrophic lateral sclerosis-parkinsonism/dementia complex of Guam or Guam disease. Amyotrophic lateral sclerosis-parkinsonism/dementia complex type 2 is a neurodengenerative disorder with unusually high incidence among the Chamorro people of the Western Pacific Islands of Guam. Both amyotrophic lateral sclerosis and parkinsonism-dementia are chronic, progressive, and uniformly fatal disorders in this population. Both diseases are known to occur in the same kindred, the same sibship, and even the same individual.
Miscellaneous	Cys-106 is easily oxidized to sulfinic acid.
Sequence similarities	Belongs to the peptidase C56 family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation Parkinson disease
Molecular function	Chaperone Oncogene
PTM	Isopeptide bond Oxidation Phosphoprotein Ubl conjugation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	Ras protein signal transduction Ref.1 Traceable author statement. Source: ProtInc
Cellular component	nucleus Ref.1 Ref.27 Inferred from direct assay. Source: MGI
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AR	P10275	5	EBI-1164361,EBI-608057
DAXX	Q9UER7	1	EBI-1164361,EBI-77321

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 189

189

Protein DJ-1

PRO_0000157849

Amino acid modifications

Modified residue

67

1

Phosphotyrosine Ref.17

Modified residue

106

1

Cysteine sulfinic acid (-SO2H)

Cross-link

130

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.18

Natural variations

Natural variant

26

1

M → I in PARK7; does not affect protein stability and degradation; does not interfere with homodimerization;. Ref.11 Ref.26

VAR_020492

Natural variant

64

1

E → D in PARK7; no apparent effect on protein stability. Ref.29 Ref.30

VAR_020493

Natural variant

98

1

R → Q Ref.26 Ref.31 Ref.28 Ref.32

VAR_020494

Natural variant

104

1

A → T in PARK7. Ref.31

VAR_020495

Natural variant

149

1

D → A in PARK7. Ref.26

VAR_020496

Natural variant

150

1

G → S Ref.8

VAR_020497

Natural variant

163

1

E → K Ref.33

VAR_034801

Natural variant

166

1

L → P in PARK7; reduces protein stability and leads to increased degradation; interferes with homodimerization; abolishes interaction with PIAS2; strongly reduces chaperone activity. Ref.10 Ref.27 Ref.11 Ref.30

VAR_020498

Natural variant

171

1

A → S Ref.31

VAR_020499

Experimental info

Mutagenesis

46

1

C → A: Reduces protein stability. No effect on oxidation. Ref.16 Ref.25

Mutagenesis

53

1

C → A: Strongly reduces chaperone activity. Ref.16 Ref.25

Mutagenesis

106

1

C → A or D: Abolishes oxidation and association with mitochondria. No effect on chaperone activity. Ref.16 Ref.25

Mutagenesis

130

1

K → R: Partially compensates for loss of stability; when associated with P-166. Ref.10

Sequence conflict

119

1

F → C in BAB71782. Ref.3

Secondary structure

1

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189

Helix Strand Turn

Details...

Beta strand

5 – 10

6

Helix

16 – 28

13

Beta strand

32 – 37

6

Beta strand

51 – 53

3

Beta strand

55 – 57

3

Helix

58 – 63

6

Beta strand

68 – 72

5

Helix

76 – 84

9

Helix

86 – 97

12

Beta strand

101 – 105

5

Turn

106 – 108

3

Helix

109 – 114

6

Helix

127 – 129

3

Helix

130 – 133

4

Turn

134 – 136

3

Beta strand

139 – 141

3

Beta strand

145 – 149

5

Beta strand

152 – 155

4

Helix

158 – 160

3

Helix

161 – 173

13

Helix

175 – 182

8

Helix

183 – 185

3

Sequences

	Sequence		Length	Mass (Da)
	Q99497-1 [UniParc]. Last modified July 5, 2004. Version 2. Checksum: 4B21661B3A76BC67	FASTA	189	19,891
	10 20 30 40 50 60 MASKRALVIL AKGAEEMETV IPVDVMRRAG IKVTVAGLAG KDPVQCSRDV VICPDASLED 70 80 90 100 110 120 AKKEGPYDVV VLPGGNLGAQ NLSESAAVKE ILKEQENRKG LIAAICAGPT ALLAHEIGFG 130 140 150 160 170 180 SKVTTHPLAK DKMMNGGHYT YSENRVEKDG LILTSRGPGT SFEFALAIVE ALNGKEVAAQ VKAPLVLKD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DJ-1, a novel oncogene which transforms mouse NIH3T3 cells in cooperation with ras." Nagakubo D., Taita T., Kitaura H., Ikeda M., Tamai K., Iguchi-Ariga S.M.M., Ariga H. Biochem. Biophys. Res. Commun. 231:509-513(1997) [PubMed: 9070310] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Cervix carcinoma.
[2]	"Homo sapiens RNA-binding protein regulatory subunit mRNA." Beaudoin R., Hod Y. Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.
[3]	"Human DJ-1 cDNA from PC3 cells." Ariga H., Niki T. Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cervix.
[6]	"Molecular cloning of human and mouse DJ-1 genes and identification of Sp1-dependent activation of the human DJ-1 promoter." Taira T., Takahashi K., Kitagawa R., Iguchi-Ariga S.M.M., Ariga H. Gene 263:285-292(2001) [PubMed: 11223268] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6. Tissue: Kidney.
[7]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 6-27; 33-89; 99-122 AND 149-175, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[8]	"DJ-1 gene G150S mutation." Zou H.Q., Chan P. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 138-189, VARIANT SER-150.
[9]	"DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor." Takahashi K., Taira T., Niki T., Seino C., Iguchi-Ariga S.M.M., Ariga H. J. Biol. Chem. 276:37556-37563(2001) [PubMed: 11477070] [Abstract] Cited for: INTERACTION WITH PIAS2, SUBCELLULAR LOCATION, FUNCTION.
[10]	"L166P mutant DJ-1, causative for recessive Parkinson's disease, is degraded through the ubiquitin-proteasome system." Miller D.W., Ahmad R., Hague S., Baptista M.J., Canet-Aviles R., McLendon C., Carter D.M., Zhu P.-P., Stadler J., Chandran J., Klinefelter G.R., Blackstone C., Cookson M.R. J. Biol. Chem. 278:36588-36595(2003) [PubMed: 12851414] [Abstract] Cited for: DEGRADATION BY THE PROTEASOME, SUBCELLULAR LOCATION, INTERACTION WITH PIAS2, HOMODIMERIZATION, MUTAGENESIS OF LYS-130, CHARACTERIZATION OF VARIANT PARK7 PRO-166.
[11]	"A missense mutation (L166P) in DJ-1, linked to familial Parkinson's disease, confers reduced protein stability and impairs homo-oligomerization." Moore D.J., Zhang L., Dawson T.M., Dawson V.L. J. Neurochem. 87:1558-1567(2003) [PubMed: 14713311] [Abstract] Cited for: DEGRADATION BY THE PROTEASOME, CHARACTERIZATION OF VARIANTS PARK7 ILE-26 AND PRO-166.
[12]	"DJBP: a novel DJ-1-binding protein, negatively regulates the androgen receptor by recruiting histone deacetylase complex, and DJ-1 antagonizes this inhibition by abrogation of this complex." Niki T., Takahashi-Niki K., Taira T., Iguchi-Ariga S.M.M., Ariga H. Mol. Cancer Res. 1:247-261(2003) [PubMed: 12612053] [Abstract] Cited for: INTERACTION WITH EFCAB6, FUNCTION.
[13]	"Immunocytochemical localization of DJ-1 in human male reproductive tissue." Yoshida K., Sato Y., Yoshiike M., Nozawa S., Ariga H., Iwamoto T. Mol. Reprod. Dev. 66:391-397(2003) [PubMed: 14579415] [Abstract] Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[14]	"DJ-1 colocalizes with tau inclusions: a link between parkinsonism and dementia." Rizzu P., Hinkle D.A., Zhukareva V., Bonifati V., Severijnen L.-A., Martinez D., Ravid R., Kamphorst W., Eberwine J.H., Lee V.M.-Y., Trojanowski J.Q., Heutink P. Ann. Neurol. 55:113-118(2004) [PubMed: 14705119] [Abstract] Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[15]	"The expression of DJ-1 (PARK7) in normal human CNS and idiopathic Parkinson's disease." Bandopadhyay R., Kingsbury A.E., Cookson M.R., Reid A.R., Evans I.M., Hope A.D., Pittman A.M., Lashley T., Canet-Aviles R., Miller D.W., McLendon C., Strand C., Leonard A.J., Abou-Sleiman P.M., Healy D.G., Ariga H., Wood N.W., de Silva R. , Revesz T., Hardy J.A., Lees A.J. Brain 127:420-430(2004) [PubMed: 14662519] [Abstract] Cited for: TISSUE SPECIFICITY.
[16]	"DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation." Shendelman S., Jonason A., Martinat C., Leete T., Abeliovich A. PLoS Biol. 2:1-10(2004) [PubMed: 15502874] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106.
[17]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67, MASS SPECTROMETRY.
[18]	"Proper SUMO-1 conjugation is essential to DJ-1 to exert its full activities." Shinbo Y., Niki T., Taira T., Ooe H., Takahashi-Niki K., Maita C., Seino C., Iguchi-Ariga S.M.M., Ariga H. Cell Death Differ. 13:96-108(2006) [PubMed: 15976810] [Abstract] Cited for: SUMOYLATION AT LYS-130, OXIDATION, SUBCELLULAR LOCATION, INDUCTION, FUNCTION.
[19]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]	"Crystal structure of DJ-1/RS and implication on familial Parkinson's disease." Huai Q., Sun Y., Wang H., Chin L.-S., Li L., Robinson H., Ke H. FEBS Lett. 549:171-175(2003) [PubMed: 12914946] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), HOMODIMERIZATION.
[21]	"Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease." Tao X., Tong L. J. Biol. Chem. 278:31372-31379(2003) [PubMed: 12761214] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF WILD-TYPE AND MUTANT ARG-130, HOMODIMERIZATION.
[22]	"The crystal structure of DJ-1, a protein related to male fertility and Parkinson's disease." Honbou K., Suzuki N.N., Horiuchi M., Niki T., Taira T., Ariga H., Inagaki F. J. Biol. Chem. 278:31380-31384(2003) [PubMed: 12796482] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), HOMODIMERIZATION.
[23]	"Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain." Lee S.-J., Kim S.J., Kim I.-K., Ko J., Jeong C.-S., Kim G.-H., Park C., Kang S.-O., Suh P.-G., Lee H.-S., Cha S.-S. J. Biol. Chem. 278:44552-44559(2003) [PubMed: 12939276] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, OXIDATION, HOMODIMERIZATION.
[24]	"The 1.1-A resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's disease." Wilson M.A., Collins J.L., Hod Y., Ringe D., Petsko G.A. Proc. Natl. Acad. Sci. U.S.A. 100:9256-9261(2003) [PubMed: 12855764] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS), HOMODIMERIZATION, OXIDATION, ABSENCE OF PROTEOLYTIC ACTIVITY.
[25]	"The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization." Canet-Aviles R.M., Wilson M.A., Miller D.W., Ahmad R., McLendon C., Bandyopadhyay S., Baptista M.J., Ringe D., Petsko G.A., Cookson M.R. Proc. Natl. Acad. Sci. U.S.A. 101:9103-9108(2004) [PubMed: 15181200] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106, OXIDATION, FUNCTION, SUBCELLULAR LOCATION.
[26]	"The role of pathogenic DJ-1 mutations in Parkinson's disease." Abou-Sleiman P.M., Healy D.G., Quinn N., Lees A.J., Wood N.W. Ann. Neurol. 54:283-286(2003) [PubMed: 12953260] [Abstract] Cited for: VARIANTS PARK7 ILE-26 AND ALA-149, VARIANT GLN-98.
[27]	"Mutations in the DJ-1 gene associated with autosomal recessive early-onset Parkinsonism." Bonifati V., Rizzu P., van Baren M.J., Schaap O., Breedveld G.J., Krieger E., Dekker M.C.J., Squitieri F., Ibanez P., Joosse M., van Dongen J.W., Vanacore N., van Swieten J.C., Brice A., Meco G., van Duijn C.M., Oostra B.A., Heutink P. Science 299:256-259(2003) [PubMed: 12446870] [Abstract] Cited for: VARIANT PARK7 PRO-166, SUBCELLULAR LOCATION.
[28]	"The R98Q variation in DJ-1 represents a rare polymorphism." Hedrich K., Schaefer N., Hering R., Hagenah J., Lanthaler A.J., Schwinger E., Kramer P.L., Ozelius L.J., Bressman S.B., Abbruzzese G., Martinelli P., Kostic V., Pramstaller P.P., Vieregge P., Riess O., Klein C. Ann. Neurol. 55:145-146(2004) [PubMed: 14705128] [Abstract] Cited for: VARIANT GLN-98.
[29]	"Novel homozygous p.E64D mutation in DJ1 in early onset Parkinson disease (PARK7)." Hering R., Strauss K.M., Tao X., Bauer A., Woitalla D., Mietz E.M., Petrovic S., Bauer P., Schaible W., Mueller T., Schoels L., Klein C., Berg D., Meyer P.T., Schulz J.B., Wollnik B., Tong L., Krueger R., Riess O. Hum. Mutat. 24:321-329(2004) [PubMed: 15365989] [Abstract] Cited for: VARIANT PARK7 ASP-64, X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[30]	"Differential effects of Parkinson's disease-associated mutations on stability and folding of DJ-1." Goerner K., Holtorf E., Odoy S., Nuscher B., Yamamoto A., Regula J.T., Beyer K., Haass C., Kahle P.J. J. Biol. Chem. 279:6943-6951(2004) [PubMed: 14607841] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS PARK7 ASP-64 AND PRO-166.
[31]	"Analysis of an early-onset Parkinson's disease cohort for DJ-1 mutations." Clark L.N., Afridi S., Mejia-Santana H., Harris J., Louis E.D., Cote L.J., Andrews H., Singleton A., Wavrant De-Vrieze F., Hardy J., Mayeux R., Fahn S., Waters C., Ford B., Frucht S., Ottman R., Marder K. Mov. Disord. 19:796-800(2004) [PubMed: 15254937] [Abstract] Cited for: VARIANT PARK7 THR-104, VARIANTS GLN-98 AND SER-171.
[32]	"DJ-1 (PARK7) mutations are less frequent than Parkin (PARK2) mutations in early-onset Parkinson disease." Hedrich K., Djarmati A., Schafer N., Hering R., Wellenbrock C., Weiss P.H., Hilker R., Vieregge P., Ozelius L.J., Heutink P., Bonifati V., Schwinger E., Lang A.E., Noth J., Bressman S.B., Pramstaller P.P., Riess O., Klein C. Neurology 62:389-394(2004) [PubMed: 14872018] [Abstract] Cited for: VARIANT GLN-98.
[33]	"DJ-1 mutations and parkinsonism-dementia-amyotrophic lateral sclerosis complex." Annesi G., Savettieri G., Pugliese P., D'Amelio M., Tarantino P., Ragonese P., La Bella V., Piccoli T., Civitelli D., Annesi F., Fierro B., Piccoli F., Arabia G., Caracciolo M., Ciro Candiano I.C., Quattrone A. Ann. Neurol. 58:803-807(2005) [PubMed: 16240358] [Abstract] Cited for: VARIANT LYS-163.
+	Additional computationally mapped references.

Web resources

GeneReviews

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBLGenBankDDBJ

D61380 mRNA. Translation: BAA09603.2.
AF021819 mRNA. Translation: AAC12806.1.
AB073864 mRNA. Translation: BAB71782.1.
AL034417 Genomic DNA. Translation: CAB52550.1.
BC008188 mRNA. Translation: AAH08188.1.
AB045294 Genomic DNA. No translation available.
AY648999 Genomic DNA. Translation: AAT68961.1.

IPI

IPI00298547.

PIR

JC5394.

RefSeq

NP_001116849.1.
NP_009193.2.

UniGene

Hs.419640

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J42	X-ray	2.50	A	1-189	[»]
1P5F	X-ray	1.10	A	1-189	[»]
1PDV	X-ray	1.80	A	1-189	[»]
1PDW	X-ray	2.20	A/B/C/D/E/F/G/H	1-189	[»]
1PE0	X-ray	1.70	A/B	1-189	[»]
1PS4	X-ray	1.60	A	1-189	[»]
1Q2U	X-ray	1.60	A	1-189	[»]
1SOA	X-ray	1.20	A	1-189	[»]
1UCF	X-ray	1.95	A/B	1-189	[»]
2OR3	X-ray	1.20	A/B	1-189	[»]
2R1T	X-ray	1.70	A	2-188	[»]
			B	2-188	[»]
2R1U	X-ray	1.50	A/B	2-188	[»]
2R1V	X-ray	1.70	A	2-188	[»]
			B	2-188	[»]
2RK3	X-ray	1.05	A	1-189	[»]
2RK4	X-ray	1.15	A	1-189	[»]
2RK6	X-ray	1.15	A	1-189	[»]
3B36	X-ray	1.50	A	1-189	[»]
3B38	X-ray	1.85	A	1-189	[»]
3B3A	X-ray	1.50	A	1-189	[»]
3BWE	X-ray	2.40	A/B/C/D/E/F/G	1-189	[»]
3CY6	X-ray	1.35	A	1-189	[»]
3CYF	X-ray	1.60	A	1-189	[»]
3CZ9	X-ray	1.15	A	1-189	[»]
3CZA	X-ray	1.20	A	1-189	[»]
3EZG	X-ray	1.15	A	1-189	[»]
3F71	X-ray	1.20	A	1-189	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q99497. 10 interactions.

Protein family/group databases

MEROPS

C56.002.

PTM databases

PhosphoSite

Q99497.

2-D gel databases

Cornea-2DPAGE

Q99497.

OGP

Q99497.

REPRODUCTION-2DPAGE

IPI00298547.

Proteomic databases

PeptideAtlas

Q99497.

PRIDE

Q99497.

Genome annotation databases

Ensembl

ENSG00000116288. Homo sapiens. [Contig view]

GeneID

11315.

KEGG

hsa:11315.

Organism-specific databases

GeneCards

GC01P007944.

H-InvDB

HIX0000097.

HGNC

HGNC:16369. PARK7.

HPA

CAB005870.
HPA004190.

MIM

105500. phenotype.
168600. phenotype.
602533. gene.
606324. phenotype.

Orphanet

2828. Parkinson disease, genetic types.

PharmGKB

PA32946.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q99497.

HOVERGEN

Q99497.

OMA

Q99497. GDHYKYS.

Enzyme and pathway databases

Pathway_Interaction_DB

alphasynuclein_pathway. Alpha-synuclein signaling.

Gene expression databases

ArrayExpress

Q99497.

Bgee

Q99497.

CleanEx

HS_PARK7.

Family and domain databases

InterPro

IPR006287. DJ1.
IPR002818. ThiJ/PfpI.
[Graphical view]

Pfam

PF01965. DJ-1_PfpI. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01383. not_thiJ. 1 hit.

ProtoNet

Search...

Other Resources

NextBio

42983.

PMAP-CutDB

Q99497.

SOURCE

Search...

Entry information

Entry name

PARK7_HUMAN

Accession

Primary (citable) accession number: Q99497
Secondary accession number(s): O14805, Q6DR95, Q7LFU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	July 5, 2004
Last modified:	June 16, 2009
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)